Journal
CHEMISTRY & BIOLOGY
Volume 18, Issue 5, Pages 642-654Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2011.03.007
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Funding
- European Union
- Wellcome Trust
- Biotechnology and Biological Research Council
- Biomedical Research Centre (NIHR), Oxford, UK
- Action Medical Research
- Swedish Research Council
- Loo and Hans Ostermans Foundation for Geriatric Research
- Foundation for Geriatric Diseases at Karolinska Institutet
- EMBO
- Fondazione Roma
- BBSRC [BB/D011523/1, BB/J003018/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/D011523/1, BB/J003018/1] Funding Source: researchfish
- British Heart Foundation [RG/11/1/28684] Funding Source: researchfish
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2-oxoglutarate (2-OG)-dependent oxygenases have diverse roles in human biology. The inhibition of several 2-OG oxygenases is being targeted for therapeutic intervention, including for cancer, anemia, and ischemic diseases. We report a small-molecule probe for 2-OG oxygenases that employs a hydroxyquinoline template coupled to a photoactivable crosslinking group and an affinity-purification tag. Following studies with recombinant proteins, the probe was shown to crosslink to 2-OG oxygenases in human crude cell extracts, including to proteins at endogenous levels. This approach is useful for inhibitor profiling, as demonstrated by crosslinking to the histone demethylase FBXL11 (KDM2A) in HEK293T nuclear extracts. The results also suggest that small-molecule probes may be suitable for substrate identification studies.
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